Ribosome Shut-Down by 16S rRNA Fragmentation in Stationary-Phase Escherichia coli. Issue 10 (22nd May 2016)

• Record Type: Journal Article
• Authors: Luidalepp, Hannes; Berger, Stefan; Joss, Oliver; Tenson, Tanel; Polacek, Norbert
• Is Part Of: Journal of molecular biology. Volume 428:Issue 10:Part B(2016:May 15)
• Page Start: 2237
• Page End: 2247
• Publication Date: 2016-05-22
• Subjects: 30S small ribosomal subunits -- 50S large ribosomal subunits -- ncRNA non-protein-coding RNA -- sRNA small non-coding RNA -- rancRNA ribosome-associated non-coding RNA -- MOPS 3-(N-morpholino)propanesulfonic acid -- DMSO dimethyl sulfoxide; 16S rRNA -- RNA cleavage -- stationary-phase bacteria -- translation -- 30S ribosomal subunits; Molecular biology -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Bacteriology -- Periodicals; Molecular Biology -- Periodicals; Biochemistry -- Periodicals; Biologie moléculaire -- Périodiques; Biologie -- Périodiques; Biochimie -- Périodiques; Moleculaire biologie; Biochemistry; Biology; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.jmb.2016.01.033
• Languages: English
• ISSNs: 0022-2836

Abstract

Abstract: Stationary-phase bacterial cells are characterized by vastly reduced metabolic activities yielding a dormant-like phenotype. Several hibernation programs ensure the establishment and maintenance of this resting growth state. Some of the stationary phase-specific modulations affect the ribosome and its translational activity directly. In stationary-phase Escherichia coli, we observed the appearance of a 16S rRNA fragmentation event at the tip of helix 6 within the small ribosomal subunit (30S). Stationary-phase 30S subunits showed markedly reduced activities in protein biosynthesis. On the other hand, the functional performance of stationary-phase large ribosomal subunits (50S) was indistinguishable from particles isolated from exponentially growing cells. Introduction of the 16S rRNA cut in vitro at helix 6 of exponential phase 30S subunits renders them less efficient in protein biosynthesis. This indicates that the helix 6 fragmentation is necessary and sufficient to attenuate translational activities of 30S ribosomal subunits. These results suggest that stationary phase-specific cleavage of 16S rRNA within the 30S subunit is an efficient means to reduce global translation activities under non-proliferating growth conditions. Graphical abstract: